ID A0A8X7X0Z5_POLSE Unreviewed; 1396 AA.
AC A0A8X7X0Z5;
DT 14-DEC-2022, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2022, sequence version 1.
DT 08-OCT-2025, entry version 12.
DE SubName: Full=COIA1 protein {ECO:0000313|EMBL:KAG2459231.1};
DE Flags: Fragment;
GN Name=Col18a1 {ECO:0000313|EMBL:KAG2459231.1};
GN ORFNames=GTO96_0019283 {ECO:0000313|EMBL:KAG2459231.1};
OS Polypterus senegalus (Senegal bichir).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Polypteriformes; Polypteridae; Polypterus.
OX NCBI_TaxID=55291 {ECO:0000313|EMBL:KAG2459231.1, ECO:0000313|Proteomes:UP000886611};
RN [1] {ECO:0000313|EMBL:KAG2459231.1, ECO:0000313|Proteomes:UP000886611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bchr_013 {ECO:0000313|EMBL:KAG2459231.1};
RX PubMed=33545088;
RA Bi X., Wang K., Yang L., Pan H., Jiang H., Wei Q., Fang M., Yu H., Zhu C.,
RA Cai Y., He Y., Gan X., Zeng H., Yu D., Zhu Y., Jiang H., Qiu Q., Yang H.,
RA Zhang Y.E., Wang W., Zhu M., He S., Zhang G.;
RT "Tracing the genetic footprints of vertebrate landing in non-teleost ray-
RT finned fishes.";
RL Cell 0:0-0(2021).
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
CC -!- SIMILARITY: Belongs to the multiplexin collagen family.
CC {ECO:0000256|ARBA:ARBA00061275}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAG2459231.1}.
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DR EMBL; JAATIS010005477; KAG2459231.1; -; Genomic_DNA.
DR Proteomes; UP000886611; Unassembled WGS sequence.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0031012; C:extracellular matrix; IEA:TreeGrafter.
DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IEA:TreeGrafter.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
DR CDD; cd00247; Endostatin-like; 1.
DR FunFam; 3.10.100.10:FF:000008; collagen alpha-1(XVIII) chain isoform X1; 1.
DR FunFam; 3.40.1620.70:FF:000003; Collagen type XVIII alpha 1; 1.
DR FunFam; 2.60.120.200:FF:000039; Collagen XV alpha 1 chain; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 3.40.1620.70; -; 1.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR050149; Collagen_superfamily.
DR InterPro; IPR010515; Collagenase_NC10/endostatin.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR048287; TSPN-like_N.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023:SF1112; COL_CUTICLE_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR Pfam; PF01391; Collagen; 4.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Reference proteome {ECO:0000313|Proteomes:UP000886611};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1396
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5036496811"
FT DOMAIN 33..221
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 219..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..1066
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1141..1212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..241
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..314
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..338
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..399
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..430
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..474
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..492
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..531
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..628
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..639
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 712..727
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..742
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 846..855
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 877..887
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 894..905
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 942..963
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1019..1034
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1047..1061
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1141..1154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KAG2459231.1"
FT NON_TER 1396
FT /evidence="ECO:0000313|EMBL:KAG2459231.1"
SQ SEQUENCE 1396 AA; 142965 MW; 2CB2000CDFBD5FC5 CRC64;
MGKRCLARLQ PLLCFVLLWS IPPVASQKGD EGDVSLLQII GDPPPEPILK VEGPDNIAGY
MFTPEVNTGQ LARAHFPAIF YRDFSLLFHI KPTSVKPGVI FAVTDFQQKL MYVGVKLSAA
KGDIRNVLFY YTEPDAESSY QAASFKISSP IDEWVRFAIK VKDDEVTFFL NCQQAEVTRI
ERSPDEMELE GGAGVFVAQA GGADPDKFEG AIAELRISGD PDLADRQCDE DEGGDDSDDA
SGDYGSGIEE KIKVQTESTI TVKPLVLPPV TKPDISVKKE KDKEKEKHKP PVAIETEKKH
VFEKVESLPP RVKEGIPAQI GLAGPKGEKG DRGEKGSRGD QGPTGPKGDN GAISTGTQGG
KGEPGEKGMK GSAGFGYPGP KGDTGAPGPP GPPGPPGPAP EVVKRGDGTV VQQVSGPQGP
PGKPGQPGAP GPAGADGEPG DPGEDGKPGT VGPPGFPGLP GDTGPKGEKG EKGEGQPGPR
GPPGPPGLPG PPRSDKQTFF DMEGSAFPDL DSIRGPPGLP GLPGPPGPPG PLSTTGTLGP
VGPPGPPGSN GKDGAPGPRG PAGLPGPPGK DGSAGQPGAK GDKGESGEYG LPGPSGEKGS
KGDTGTPGNP GEIGLAGLPG PMGPVGLPGL PGPPGPPGPG FAFGIDDTEG SAFGVSGPDG
KPGLPGVPGM PGLKGDRGIP GLPGLKGESG IPGAAGKDGQ QGLDGFPGPE GLKGDKGDPG
ERGEPGRDGA GLPGPPGPPG PPGRTIYEAS ENHGFNGVPG PEGKQGVNGQ AGFPGPMGPK
GDRGDRGPPG YGIKGEKGEP GSLIGPDGNI MNGYLSRAAK GEKGDRGPPG PFGPVGATGH
KGEIGLPGRP GRPGLNGFKG EKGEPADPSG RYAVVGPPGP PGPPGPPGIA GYDETGGAGR
VLTGGKGERG FPGYPGEKGE PGEPGQPGLP GQPGSLSNFD VHSLKRELKG ERGDVGLKGE
KGEPGGGGGY YDSRFSGIQG PPGKPGPQGL PGPKGDSIRG PPGPPGHQGP PGVGYDGRPG
PPGQPGLPGP PGPSASPGAS RHSISIPGPP GPQGPPGPPG YPSGVNIVRN LQTMMSTARN
VQEGTLIMIL EKGDLYIRVR DGYRQIMLGE YTPFFGPGGG IFENEVAAVQ PPPVILYPHS
HPSQSAAETI SQGGQDIKQD LPPHSPVRQP DYGHNVYPSV PDPPRRNPLL PQVSYPDSPQ
HRPHLSESSS SAIHLHGTGP ALHLIALNSP QTGDMRGIRG ADFQCFQQAR AVGLTGTFRA
FLSSKLQDLY SIVRRADRNT LPIVNLKDEV LFDSWESLYN GLDGQMKPNV HIYSFDGRDV
LKDNTWTQKM VWHGSNNKGQ RMTDHYCETW RTGVHELTGF ASSLEAGRLL QQRPVSCSSS
LIVLCIENSF MTQAKK
//
